ALDH2_MESAU
ID ALDH2_MESAU Reviewed; 500 AA.
AC P81178;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Aldehyde dehydrogenase, mitochondrial;
DE EC=1.2.1.3;
DE AltName: Full=ALDH class 2;
DE AltName: Full=ALDH-E2;
DE AltName: Full=ALDH1;
GN Name=ALDH2;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=9369242; DOI=10.1016/s0014-5793(97)01176-9;
RA Hjelmqvist L., Lundgren R., Norin A., Joernvall H., Vallee B., Klyosov A.,
RA Keung W.M.;
RT "Class 2 aldehyde dehydrogenase. Characterization of the hamster enzyme,
RT sensitive to daidzin and conserved within the family of multiple forms.";
RL FEBS Lett. 416:99-102(1997).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 2/2.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P81178; -.
DR SMR; P81178; -.
DR STRING; 10036.XP_005080704.1; -.
DR eggNOG; KOG2450; Eukaryota.
DR SABIO-RK; P81178; -.
DR UniPathway; UPA00780; UER00768.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; ISS:UniProtKB.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR GO; GO:0018547; F:nitroglycerin reductase activity; ISS:UniProtKB.
DR GO; GO:0008957; F:phenylacetaldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0046185; P:aldehyde catabolic process; ISS:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1903179; P:regulation of dopamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:1905627; P:regulation of serotonin biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..500
FT /note="Aldehyde dehydrogenase, mitochondrial"
FT /id="PRO_0000056468"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 302
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 245..250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 169
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 351
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 358
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 366
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 390
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 409
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 411
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 424
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
FT MOD_RES 434
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47738"
SQ SEQUENCE 500 AA; 54334 MW; 8B81886AB04F493F CRC64;
SAAATSAVPA PNQQPEVFCN QIFINNEWHD AVSKKTFPTV NPSTGEVICQ VAEGSKEDVD
KAVKAARAAF QLGSPWRRMD ASDRGRLLNR LADLIERDRT YLAALETLDN GKPYVISYLV
DLDMVLKCLR YYAGWADKYH GKTIPIDGDF FSYTRHEPVG VCGQIIPWNF PLLMQAWKLG
PALATGNVVV MKVAEQTPLT ALYVANLIKE AGFPPGVVNI VPGFGPTAGA AIASHEDVDK
VAFTGSTEVG HLIQVAAGSS NLKRVTLELG GKSPNIIMSD ADMDWAVEQA HFALFFNQGQ
CCCAGSRTFV QEDVYDEFVE RSVARAKSRV VGNPFDSRTE QGPQVDETQF KKILGYIKSG
QQEGAKLLCG GGAAADRGYF IQPTVFGDVK DGMTIAKEEI FGPVMQILKF KTIEEVVGRA
NNSKYGLAAA VFTKDLDKAN YLSQALQAGT VWINCYDVFG AQSPFGGYKM SGSGRELGEY
GLQAYTEVKT VTIKVPQKNS
